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Literature summary extracted from

  • Guan, H.; Song, S.; Robinson, H.; Liang, J.; Ding, H.; Li, J.; Han, Q.
    Structural basis of the substrate specificity and enzyme catalysis of a Papaver somniferum tyrosine decarboxylase (2017), Front. Mol. Biosci., 4, 5-5 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.25 gene tdc, recombinant expression of tagged enzyme Papaver somniferum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.25 purified recombinant tagged enzyme, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 25 mM HEPES, pH 7.0, and 0.04 mM pyridoxal 5'-phosphate, with 0.001 ml of reservoir solution containing 0.2 M NaOAc and 1 M NH4H2PO4, and equilibration against 0.45 ml of reservoir solution, X-ray diffraction structure determination and analysis at 3.1 A resolution Papaver somniferum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.25 L-Tyrosine Papaver somniferum
-
 Tyramine + CO2
-
 ?
4.1.1.25 additional information Papaver somniferum TDC catalyzes the decarboxylation of tryptophan to tryptamine and 5-hydroxytryptophan to serotonin. Tryptophan is a good ligand showing the highest binding affinity. Tyrosine and dopa show the same binding affinity only slightly lower as tryptophan ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.25 Papaver somniferum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.25 recombinant tagged enzyme by affinity and anion exchange chromatography, and gel filtration Papaver somniferum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.25 L-Tyrosine
-
 Papaver somniferum Tyramine + CO2
-
 ?
4.1.1.25 additional information TDC catalyzes the decarboxylation of tryptophan to tryptamine and 5-hydroxytryptophan to serotonin. Tryptophan is a good ligand showing the highest binding affinity. Tyrosine and dopa show the same binding affinity only slightly lower as tryptophan Papaver somniferum ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.25 dimer
-
 Papaver somniferum

Synonyms

EC Number Synonyms Comment Organism
4.1.1.25 TYDC
-
 Papaver somniferum
4.1.1.25 Tydc9
-
 Papaver somniferum

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.25 pyridoxal 5'-phosphate PLP, binding structure, overview. The cofactor is covalently attached to the epsilon-amino group of K321 to form an internal aldimine via a Schiff-base interaction. The protonated pyridine nitrogen of PLP forms a pair of salt bridges to the carboxyl group of D289. The PLP pyridine ring is anchored by the methyl group of A291 and the imidazole ring of H205. The O3 atom of the pyridine ring of PLP seems to interact with T264 adjacent water molecules. The phosphate moiety of PLP is stabilized by a number of interactions with T169, C170, N318 of one subunit, and R373 of the other subunit Papaver somniferum

General Information

EC Number General Information Comment Organism
4.1.1.25 evolution tyrosine decarboxylase (TyDC) is a member of aromatic amino acid decarboxylases (AAADs), which are a group of phylogenetically diverse enzymes grouped together based on their pyridoxal 5'-phosphate (PLP) dependence and sequence homology. Tyrosine decarboxylase (TyDC) is a type II pyridoxal 5'-phosphate decarboxylase that has a generally high sequence identity to other aromatic amino acid decarboxylases (AAADs) Papaver somniferum
4.1.1.25 additional information structural basis of the substrate selectivity of enzyme TyDC9, crystal structure analysis, and molecular docking of tyrosine, dopa, tyrosine, tryptophan into the active site and simulation revealing the substrate binding sites and the residues required for conformational stability, active site analysis, overview Papaver somniferum